eF-site ID 4pu3-ABCD PDB Code 4pu3 Chain A, B, C, D click to enlarge Title Shewanella oneidensis MR-1 Toxin Antitoxin System HipA, HipB and its operator DNA complex (space group P212121) Classification TOXIN/ANTITOXIN/DNA Compound Toxin-antitoxin system toxin HipA family Source Shewanella oneidensis (strain MR-1) (4PU3) Sequence A:  TLEMHLGDLMIGELSFDATADTFAVHYTKDWQQSGFPLSP TIPLDGTGTSNQISMFLVNLLPENKGLDYLIESLGVSKGN TFALIRAIGLDTAGAIAFVPKGALLPETQLRPIKAEEVIQ RIEDPTMWPMEIWDGKPRLXVAGVQPKLNLFYNGKEFAFA EGTLSSTHIVKFEKYHHLVINEFITMRLAKVLGMNVANVD IVHFGRYKALCVERFDRRNIPGEQRVLRRHIVDSCQALGF SVSKKYERNFGTGRDVKDIREGVSFNRLFSLAAKCRNPVA AKQDMLQWALFNLLTGNADAHGKNYSFFMTPSGMEPTPWY DLVSVDMYEDFEQQLAMAIDDEFDPNSIYAYQLAAFMDGL GLPRNLLISNLTRIARRIPQAIAEVILMLPPLDEDEASFV AHYKTQLLARCERYLGFVDEVRDVEV B:  TLEMHLGDLMIGELSFDATADTFAVHYTKDWQQSGFPLSP TIPLDGTGTSNQISMFLVNLLPENKGLDYLIESLGVSKGN TFALIRAIGLDTAGAIAFVPKGALLPETQLRPIKAEEVIQ RIEDPTMWPMEIWDGKPRLXVAGVQPKLNLFYNGKEFAFA EGTLSSTHIVKFEKYHHLVINEFITMRLAKVLGMNVANVD IVHFGRYKALCVERFDRRNIPGEQRVLRRHIVDSCQALGF SVSKKYERNFGTGRDVKDIREGVSFNRLFSLAAKCRNPVA AKQDMLQWALFNLLTGNADAHGKNYSFFMTPSGMEPTPWY DLVSVDMYEDFEQQLAMAIDDEFDPNSIYAYQLAAFMDGL GLPRNLLISNLTRIARRIPQAIAEVILMLPPLDEDEASFV AHYKTQLLARCERYLGFVDEVRDVEV C:  IMASPLNQQSLGLLIKERRKSAALTQDVAAMLCGVTKKTL IRVEKGEDVYISTVFKILDGLGIDIVSAGWY D:  IMASPLNQQSLGLLIKERRKSAALTQDVAAMLCGVTKKTL IRVEKGEDVYISTVFKILDGLGIDIVSAGWY Description Functional site 1) chain D residue 44-63 type DNA_BIND sequence QDVAAMLCGVTKKTLIRVEK description H-T-H motif => ECO:0000255|PROSITE-ProRule:PRU00257, ECO:0000269|PubMed:25056321 source Swiss-Prot : SWS_FT_FI1 2) chain C residue 44-63 type DNA_BIND sequence QDVAAMLCGVTKKTLIRVEK description H-T-H motif => ECO:0000255|PROSITE-ProRule:PRU00257, ECO:0000269|PubMed:25056321 source Swiss-Prot : SWS_FT_FI1 3) chain B residue 380-384 type DNA_BIND sequence RIARR description H-T-H motif => ECO:0000255|PROSITE-ProRule:PRU00257, ECO:0000269|PubMed:25056321 source Swiss-Prot : SWS_FT_FI1 4) chain B residue 429 type DNA_BIND sequence R description H-T-H motif => ECO:0000255|PROSITE-ProRule:PRU00257, ECO:0000269|PubMed:25056321 source Swiss-Prot : SWS_FT_FI1 5) chain A residue 306 type ACT_SITE sequence D description Proton acceptor => ECO:0000250|UniProtKB:P23874 source Swiss-Prot : SWS_FT_FI2 6) chain B residue 306 type ACT_SITE sequence D description Proton acceptor => ECO:0000250|UniProtKB:P23874 source Swiss-Prot : SWS_FT_FI2 7) chain A residue 151 type BINDING sequence V description BINDING => ECO:0000269|PubMed:25056321 source Swiss-Prot : SWS_FT_FI3 8) chain B residue 327 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:25056321 source Swiss-Prot : SWS_FT_FI3 9) chain A residue 178 type BINDING sequence K description BINDING => ECO:0000269|PubMed:25056321 source Swiss-Prot : SWS_FT_FI3 10) chain A residue 220 type BINDING sequence E description BINDING => ECO:0000269|PubMed:25056321 source Swiss-Prot : SWS_FT_FI3 11) chain A residue 308 type BINDING sequence H description BINDING => ECO:0000269|PubMed:25056321 source Swiss-Prot : SWS_FT_FI3 12) chain A residue 327 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:25056321 source Swiss-Prot : SWS_FT_FI3 13) chain B residue 151 type BINDING sequence V description BINDING => ECO:0000269|PubMed:25056321 source Swiss-Prot : SWS_FT_FI3 14) chain B residue 178 type BINDING sequence K description BINDING => ECO:0000269|PubMed:25056321 source Swiss-Prot : SWS_FT_FI3 15) chain B residue 220 type BINDING sequence E description BINDING => ECO:0000269|PubMed:25056321 source Swiss-Prot : SWS_FT_FI3 16) chain B residue 308 type BINDING sequence H description BINDING => ECO:0000269|PubMed:25056321 source Swiss-Prot : SWS_FT_FI3 17) chain A residue 147 type MOD_RES sequence X description Phosphoserine; by autocatalysis => ECO:0000269|PubMed:25056321 source Swiss-Prot : SWS_FT_FI4 18) chain B residue 147 type MOD_RES sequence X description Phosphoserine; by autocatalysis => ECO:0000269|PubMed:25056321 source Swiss-Prot : SWS_FT_FI4

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